1ms3: Difference between revisions
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<StructureSection load='1ms3' size='340' side='right'caption='[[1ms3]], [[Resolution|resolution]] 1.65Å' scene=''> | <StructureSection load='1ms3' size='340' side='right'caption='[[1ms3]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ms3]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ms3]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Trycr Trycr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MS3 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mr5|1mr5]], [[1ms0|1ms0]], [[1ms1|1ms1]], [[1ms4|1ms4]], [[1ms5|1ms5]], [[1ms8|1ms8]], [[1ms9|1ms9]], [[1mz5|1mz5]], [[1mz6|1mz6]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mr5|1mr5]], [[1ms0|1ms0]], [[1ms1|1ms1]], [[1ms4|1ms4]], [[1ms5|1ms5]], [[1ms8|1ms8]], [[1ms9|1ms9]], [[1mz5|1mz5]], [[1mz6|1mz6]]</div></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Exo-alpha-sialidase Exo-alpha-sialidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.18 3.2.1.18] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ms3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ms3 OCA], [https://pdbe.org/1ms3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ms3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ms3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ms3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 09:55, 25 August 2021
Monoclinic form of Trypanosoma cruzi trans-sialidaseMonoclinic form of Trypanosoma cruzi trans-sialidase
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTrans-sialidases (TS) are GPI-anchored surface enzymes expressed in specific developmental stages of trypanosome parasites like Trypanosoma cruzi, the etiologic agent of Chagas disease, and T. brucei, the causative agent of sleeping sickness. TS catalyzes the transfer of sialic acid residues from host to parasite glycoconjugates through a transglycosidase reaction that appears to be critical for T. cruzi survival and cell invasion capability. We report here the structure of the T. cruzi trans-sialidase, alone and in complex with sugar ligands. Sialic acid binding is shown to trigger a conformational switch that modulates the affinity for the acceptor substrate and concomitantly creates the conditions for efficient transglycosylation. The structure provides a framework for the structure-based design of novel inhibitors with potential therapeutic applications. The crystal structure and mode of action of trans-sialidase, a key enzyme in Trypanosoma cruzi pathogenesis.,Buschiazzo A, Amaya MF, Cremona ML, Frasch AC, Alzari PM Mol Cell. 2002 Oct;10(4):757-68. PMID:12419220[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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